Phenoloxidase subunit 2 precursor - Bombyx mori (Silk moth)

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Reviewed, UniProtKB/Swiss-Prot Q27452 (PRP2_BOMMO)

Last modified May 5, 2009. Version 53. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names	Recommended name: Phenoloxidase subunit 2 EC=1.14.18.1 Alternative name(s): Tyrosinase 2 PO 2
Organism	Bombyx mori (Silk moth)
Taxonomic identifier	7091 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Bombycoidea › Bombycidae › Bombycinae › Bombyx

Protein attributes

Sequence length	693 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone. Ref.1
Catalytic activity	L-tyrosine + L-dopa + O₂ = L-dopa + dopaquinone + H₂O. Ref.1
Cofactor	Binds 2 copper ions per subunit By similarity. UniProtKB P04253
Subunit structure	Heterodimer. Ref.1
Subcellular location	Secreted.
Tissue specificity	Synthesized by hemocytes and released into the hemolymph plasma. Ref.1
Post-translational modification	The N-terminus is blocked. Ref.3
Sequence similarities	Belongs to the tyrosinase family.
Mass spectrometry	Molecular mass is 81105 Da from positions 52 - 693. Determined by MALDI. Ref.3

Ontologies

Keywords
Biological process	Melanin biosynthesis
Cellular component	Secreted
Ligand	Copper Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Glycoprotein Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	defense response Ref.1 Traceable author statement. Source: UniProtKB melanin biosynthetic process from tyrosine Ref.1 Traceable author statement. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Ref.1 Traceable author statement. Source: UniProtKB
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW monophenol monooxygenase activity Ref.1 Traceable author statement. Source: UniProtKB oxygen transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

51

PRO_0000035901

Chain

642

Phenoloxidase subunit 2 Ref.1

PRO_0000035902

Sites

Metal binding

1

Copper A By similarity UniProtKB P04253

Metal binding

1

Copper A By similarity UniProtKB P04253

Metal binding

1

Copper A By similarity UniProtKB P04253

Metal binding

1

Copper B By similarity UniProtKB P04253

Metal binding

1

Copper B By similarity UniProtKB P04253

Metal binding

1

Copper B By similarity UniProtKB P04253

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

1

P → Q AA sequence Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q27452-1 [UniParc].

Last modified January 1, 1999. Version 2.
Checksum: 013114DF4CC1A926
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693

80,119

        10         20         30         40         50         60 
MADVFESLEL LFDRPNEPLI TPKGENNSVF QLTEQFLTED YANNGIELNN RFGDDASEKI 

        70         80         90        100        110        120 
PLKNLSKLPE FKIATQLPKD AEFSLFLPKH QEMANELLGV LMDVPENELQ DLLSTCAFAR 

       130        140        150        160        170        180 
VNLNPQLFNY CYSVALMHRR DTRKVRVKNF AEVFPSKFLD SQVFTQARET AAVIPPDVPR 

       190        200        210        220        230        240 
IPIIIPRDYT ATDLEEEHRL AYWREDIGIN LHHYHWHLVY PFTANDLSIV AKDRRGELFF 

       250        260        270        280        290        300 
YMHQQVIARF NCERLCNSLK RVKKFSNWRE PIPEAYFPKL DSLTSSRGWP PRQSGMQWQD 

       310        320        330        340        350        360 
LNRAAEGLFV TIDEMERWRR NVEEAIATGT VRLPNGQTRP LDIDTLGNML ESSALSPNRE 

       370        380        390        400        410        420 
LYGSIHNNGH SFTAYMHDPE HRYLEQFGVI ADEATTMRDP FFYRWHAYID DVFQKHKESA 

       430        440        450        460        470        480 
YVRPYTRSEL ENPGVQVRSV SVETPGGQPN TLNTFWMLSD VNLSRGLDFS DNGPVYARFT 

       490        500        510        520        530        540 
HLNYRHFSYR INVNNTGSSR RTTVRIFITP KFDERNVPWI FSDQRKMCIE MDRFVTVLNA 

       550        560        570        580        590        600 
GENNIVRQST ESSITIPFEQ TFRDLSAQGN DPRRDELATF NYCGCGWPQH MLVPKGTEAG 

       610        620        630        640        650        660 
MPFQLFVMLS NYDLDRIDQD DGKQLTCVEA SSFCGLKDKK YPDRRAMGFP FDRPSSSATS 

       670        680        690 
LQDFILPNMG LQDITIQLQN VTEPNPRNPP MSV

References

[1]	"Molecular cloning of insect pro-phenol oxidase: a copper-containing protein homologous to arthropod hemocyanin." Kawabata T., Yasuhara Y., Ochiai M., Matsuura S., Ashida M. Proc. Natl. Acad. Sci. U.S.A. 92:7774-7778(1995) [PubMed: 7644494] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: Kinshu X Showa. Tissue: Hemocyte.
[2]	Asano T., Ashida M. Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Reexamination of properties of phenoloxidase isolated from larval hemolymph of the silkworm Bombyx mori." Yasuhara Y., Koizumi Y., Katagiri C., Ashida M. Arch. Biochem. Biophys. 320:14-23(1995) [PubMed: 7793973] [Abstract] Cited for: MASS SPECTROMETRY. Tissue: Hemocyte.

Cross-references

Sequence databases
	D49371 mRNA. Translation: BAA08369.1. AB048762 mRNA. Translation: BAB41101.1.
RefSeq	NP_001037534.1.
UniGene	Bmo.1389
3D structure databases
HSSP	HSSP built from PDB template 1OXY based on UniProtKB P04253.
ModBase	Search...
Genome annotation databases
GeneID	693073.
Enzyme and pathway databases
BRENDA	1.14.18.1. 252.
Family and domain databases
InterPro	IPR008922. Di-copper_centre. IPR013788. Hemocyanin. IPR005203. Hemocyanin_C. IPR000896. Hemocyanin_Cu. IPR005204. Hemocyanin_N. IPR002227. Tyrosinase. [Graphical view]
Gene3D	G3DSA:1.10.1280.10. Di-copper_centre. 1 hit. G3DSA:2.60.40.1520. hemocyanin_C. 1 hit. G3DSA:1.20.1370.10. hemocyanin_N. 1 hit.
PANTHER	PTHR11511. Hemocyanin. 1 hit.
Pfam	PF03723. Hemocyanin_C. 1 hit. PF00372. Hemocyanin_M. 1 hit. PF03722. Hemocyanin_N. 1 hit. [Graphical view]
PRINTS	PR00187. HAEMOCYANIN.
PROSITE	PS00209. HEMOCYANIN_1. 1 hit. PS00210. HEMOCYANIN_2. 1 hit. PS00497. TYROSINASE_1. False negative. PS00498. TYROSINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PRP2_BOMMO

Accession

Primary (citable) accession number: Q27452

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	January 1, 1999
Last modified:	May 5, 2009
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents